Molecular chaperones as regulators of cell death.
Molecular chaperones have been reported as multifunctional antistress molecules that can regulate diverse biological processes to maintain cellular homeostasis. Molecular chaperones have critical roles for maintaining proper protein folding, protein translocation, degradation of unfolded protein, regulating signal-transduction proteins and so on. Under pathological conditions, inducible or constitutively expressed molecular chaperones protect cells from stress. Non-dividing terminally differentiated cells accumulate abnormal proteins due to chronic environmental or physiological stress; thus, proper chaperone function is critical for maintaining homeostasis of those cells, such as neuronal and muscular cells. Cancer cells also have overexpression of molecular chaperone proteins for promoting survival from stress related to growth, cell cycle, hypoxia, metastasis and genetic mutations. Here, we will focus on the function of molecular chaperone proteins for the regulation of cell death in degenerative diseases, ischemic diseases and in cancer.
Hishiya
A
A
Cardiovascular Program, The Boston Biomedical Research Institute, Watertown, MA 02472, USA.
Takayama
S
S
D000818:Animals; D016923:Cell Death / Q000502:physiology*; D006801:Humans; D007511:Ischemia / Q000378:metabolism / Q000473:pathology; D051379:Mice; D018832:Molecular Chaperones / Q000378:metabolism / Q000502:physiology*; D009369:Neoplasms / Q000378:metabolism / Q000473:pathology; D019636:Neurodegenerative Diseases / Q000378:metabolism / Q000473:pathology
D018832:Molecular Chaperones